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Myosin-2 (Cell division control protein 66) (Class V unconventional myosin MYO2) (Type V myosin heavy chain MYO2) (Myosin V MYO2)

 MYO2_YEAST              Reviewed;        1574 AA.
P19524; D6W323;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 1.
23-MAY-2018, entry version 199.
RecName: Full=Myosin-2;
AltName: Full=Cell division control protein 66;
AltName: Full=Class V unconventional myosin MYO2;
AltName: Full=Type V myosin heavy chain MYO2;
Short=Myosin V MYO2;
Name=MYO2; Synonyms=CDC66; OrderedLocusNames=YOR326W; ORFNames=O6167;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=S288c / GRF88;
PubMed=2016335; DOI=10.1083/jcb.113.3.539;
Johnston G.C., Prendergast J.A., Singer R.A.;
"The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin
for vectorial transport of vesicles.";
J. Cell Biol. 113:539-551(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169874;
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
Nature 387:98-102(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-748.
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=8896266;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<1021::AID-YEA981>3.3.CO;2-Z;
Pearson B.M., Hernando Y., Payne J., Wolf S.S., Kalogeropoulos A.,
Schweizer M.;
"Sequencing of a 35.71 kb DNA segment on the right arm of yeast
chromosome XV reveals regions of similarity to chromosomes I and
XIII.";
Yeast 12:1021-1031(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 677-1574.
PubMed=8896263;
DOI=10.1002/(SICI)1097-0061(199609)12:10B<999::AID-YEA976>3.0.CO;2-E;
Parle-McDermott A.G., Hand N.J., Goulding S.E., Wolfe K.H.;
"Sequence of 29 kb around the PDR10 locus on the right arm of
Saccharomyces cerevisiae chromosome XV: similarity to part of
chromosome I.";
Yeast 12:999-1004(1996).
[6]
INTERACTION WITH CMD1.
PubMed=8294515; DOI=10.1083/jcb.124.3.315;
Brockerhoff S.E., Stevens R.C., Davis T.N.;
"The unconventional myosin, Myo2p, is a calmodulin target at sites of
cell growth in Saccharomyces cerevisiae.";
J. Cell Biol. 124:315-323(1994).
[7]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-511.
PubMed=8188749; DOI=10.1083/jcb.125.4.825;
Lillie S.H., Brown S.S.;
"Immunofluorescence localization of the unconventional myosin, Myo2p,
and the putative kinesin-related protein, Smy1p, to the same regions
of polarized growth in Saccharomyces cerevisiae.";
J. Cell Biol. 125:825-842(1994).
[8]
INTERACTION WITH MLC1.
PubMed=9700160; DOI=10.1083/jcb.142.3.711;
Stevens R.C., Davis T.N.;
"Mlc1p is a light chain for the unconventional myosin Myo2p in
Saccharomyces cerevisiae.";
J. Cell Biol. 142:711-722(1998).
[9]
MUTAGENESIS OF GLY-1248.
PubMed=9843969; DOI=10.1073/pnas.95.25.14799;
Catlett N.L., Weisman L.S.;
"The terminal tail region of a yeast myosin-V mediates its attachment
to vacuole membranes and sites of polarized growth.";
Proc. Natl. Acad. Sci. U.S.A. 95:14799-14804(1998).
[10]
INTERACTION WITH RHO3.
PubMed=10207081; DOI=10.1128/MCB.19.5.3580;
Robinson N.G.G., Guo L., Imai J., Toh-e A., Matsui Y., Tamanoi F.;
"Rho3 of Saccharomyces cerevisiae, which regulates the actin
cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and
Exo70.";
Mol. Cell. Biol. 19:3580-3587(1999).
[11]
FUNCTION, AND MUTAGENESIS OF ASP-1297; LEU-1301; ASN-1304 AND
ASN-1307.
PubMed=10931864; DOI=10.1083/jcb.150.3.513;
Catlett N.L., Duex J.E., Tang F., Weisman L.S.;
"Two distinct regions in a yeast myosin-V tail domain are required for
the movement of different cargoes.";
J. Cell Biol. 150:513-526(2000).
[12]
INTERACTION WITH SMY1.
PubMed=10679024; DOI=10.1091/mbc.11.2.691;
Beningo K.A., Lillie S.H., Brown S.S.;
"The yeast kinesin-related protein Smy1p exerts its effects on the
class V myosin Myo2p via a physical interaction.";
Mol. Biol. Cell 11:691-702(2000).
[13]
INTERACTION WITH KAR9.
PubMed=10984058; DOI=10.1038/35023024;
Yin H., Pruyne D., Huffaker T.C., Bretscher A.;
"Myosin V orientates the mitotic spindle in yeast.";
Nature 406:1013-1015(2000).
[14]
FUNCTION.
PubMed=11285273; DOI=10.1083/jcb.153.1.47;
Rossanese O.W., Reinke C.A., Bevis B.J., Hammond A.T., Sears I.B.,
O'Connor J., Glick B.S.;
"A role for actin, Cdc1p, and Myo2p in the inheritance of late Golgi
elements in Saccharomyces cerevisiae.";
J. Cell Biol. 153:47-62(2001).
[15]
FUNCTION.
PubMed=11381095; DOI=10.1083/jcb.153.5.1121;
Reck-Peterson S.L., Tyska M.J., Novick P.J., Mooseker M.S.;
"The yeast class V myosins, Myo2p and Myo4p, are nonprocessive actin-
based motors.";
J. Cell Biol. 153:1121-1126(2001).
[16]
ERRATUM.
Reck-Peterson S.L., Tyska M.J., Novick P.J., Mooseker M.S.;
J. Cell Biol. 153:1521-1521(2001).
[17]
FUNCTION.
PubMed=11733545; DOI=10.1083/jcb.200107028;
Hoepfner D., van den Berg M., Philippsen P., Tabak H.F., Hettema E.H.;
"A role for Vps1p, actin, and the Myo2p motor in peroxisome abundance
and inheritance in Saccharomyces cerevisiae.";
J. Cell Biol. 155:979-990(2001).
[18]
INTERACTION WITH MLC1 AND SEC4.
PubMed=12456647; DOI=10.1093/emboj/cdf650;
Wagner W., Bielli P., Wacha S., Ragnini-Wilson A.;
"Mlc1p promotes septum closure during cytokinesis via the IQ motifs of
the vesicle motor Myo2p.";
EMBO J. 21:6397-6408(2002).
[19]
FUNCTION.
PubMed=11781333; DOI=10.1083/jcb.200110086;
Schott D.H., Collins R.N., Bretscher A.;
"Secretory vesicle transport velocity in living cells depends on the
myosin-V lever arm length.";
J. Cell Biol. 156:35-39(2002).
[20]
FUNCTION, INTERACTION WITH YPT11, AND MUTAGENESIS OF VAL-1189;
VAL-1288; LEU-1474; GLU-1484; LYS-1500; ASP-1511; PRO-1529; GLU-1546
AND LYS-1559.
PubMed=12391144; DOI=10.1128/MCB.22.22.7744-7757.2002;
Itoh T., Watabe A., Toh-e A., Matsui Y.;
"Complex formation with Ypt11p, a rab-type small GTPase, is essential
to facilitate the function of Myo2p, a class V myosin, in
mitochondrial distribution in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 22:7744-7757(2002).
[21]
INTERACTION WITH SHE4.
PubMed=12725728; DOI=10.1016/S0960-9822(03)00264-1;
Wesche S., Arnold M., Jansen R.-P.;
"The UCS domain protein She4p binds to myosin motor domains and is
essential for class I and class V myosin function.";
Curr. Biol. 13:715-724(2003).
[22]
INTERACTION WITH VAC17, AND MUTAGENESIS OF SER-1247; VAL-1262;
PHE-1264; SER-1268; THR-1274; PHE-1275 AND VAL-1288.
PubMed=12642614; DOI=10.1083/jcb.200210139;
Ishikawa K., Catlett N.L., Novak J.L., Tang F., Nau J.J.,
Weisman L.S.;
"Identification of an organelle-specific myosin V receptor.";
J. Cell Biol. 160:887-897(2003).
[23]
FUNCTION.
PubMed=12743102; DOI=10.1083/jcb.200302030;
Hwang E., Kusch J., Barral Y., Huffaker T.C.;
"Spindle orientation in Saccharomyces cerevisiae depends on the
transport of microtubule ends along polarized actin cables.";
J. Cell Biol. 161:483-488(2003).
[24]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[25]
INTERACTION WITH MMR1.
PubMed=15201867; DOI=10.1038/sj.emboj.7600271;
Itoh T., Toh-e A., Matsui Y.;
"Mmr1p is a mitochondrial factor for Myo2p-dependent inheritance of
mitochondria in the budding yeast.";
EMBO J. 23:2520-2530(2004).
[26]
INTERACTION WITH SRO7.
PubMed=15964280; DOI=10.1016/j.cub.2005.05.046;
Gangar A., Rossi G., Andreeva A., Hales R., Brennwald P.;
"Structurally conserved interaction of Lgl family with SNAREs is
critical to their cellular function.";
Curr. Biol. 15:1136-1142(2005).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1097 AND SER-1121, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[30]
FUNCTION, AND INTERACTION WITH SRO7.
PubMed=21248204; DOI=10.1091/mbc.E10-07-0570;
Rossi G., Brennwald P.;
"Yeast homologues of lethal giant larvae and type V myosin cooperate
in the regulation of Rab-dependent vesicle clustering and polarized
exocytosis.";
Mol. Biol. Cell 22:842-857(2011).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[32]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 806-878 IN COMPLEX WITH
MLC1.
PubMed=12351846; DOI=10.1107/S0907444902013951;
Terrak M., Otterbein L.R., Wu G., Palecanda L.A., Lu R.C.,
Dominguez R.;
"Crystallization, X-ray characterization and selenomethionine phasing
of Mlc1p bound to IQ motifs from myosin V.";
Acta Crystallogr. D 58:1882-1885(2002).
[33]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 806-830 AND 854-878 IN
COMPLEX WITH MLC1.
PubMed=12554638; DOI=10.1093/emboj/cdg058;
Terrak M., Wu G., Stafford W.F., Lu R.C., Dominguez R.;
"Two distinct myosin light chain structures are induced by specific
variations within the bound IQ motifs-functional implications.";
EMBO J. 22:362-371(2003).
-!- FUNCTION: Myosin heavy chain that is required for the cell cycle-
regulated transport of various organelles and proteins for their
segregation. Functions by binding with its tail domain to receptor
proteins on organelles and exerting force with its N-terminal
motor domain against actin filaments, thereby transporting its
cargo along polarized actin cables. Essential for the delivery of
secretory vesicles to sites of active growth during bud emergence
and cytokinesis. Required for segregation and inheritance of
peroxisomes, late Golgi compartments, mitochondria and the vacuole
to the daughter cell during cell division. Also required for
correct alignment of the spindle during mitosis.
{ECO:0000269|PubMed:10931864, ECO:0000269|PubMed:11285273,
ECO:0000269|PubMed:11381095, ECO:0000269|PubMed:11733545,
ECO:0000269|PubMed:11781333, ECO:0000269|PubMed:12391144,
ECO:0000269|PubMed:12743102, ECO:0000269|PubMed:21248204}.
-!- SUBUNIT: Homodimer. Interacts with calmodulin (CMD1) and the
myosin light chain MLC1 through its IQ repeats. Binds to the
membrane receptors SEC4 and VAC17 to transport secretory vesicles
and the vacuole, respectively. Binds to KAR9, which transports
BIM1-coated cytoplasmic microtubules that are attached to the
spindle pole body into the emerging bud, thereby correctly
orienting the mitotic spindle. Interacts with YPT11 and MMR1 to
accelerate mitochondrial distribution to the bud. Interacts with
SHE4 and localizes it to the bud tip. Interacts with RHO3 and
SMY1, putative regulators of MYO2 function. Interacts with SRO7.
{ECO:0000269|PubMed:10207081, ECO:0000269|PubMed:10679024,
ECO:0000269|PubMed:10984058, ECO:0000269|PubMed:12351846,
ECO:0000269|PubMed:12391144, ECO:0000269|PubMed:12456647,
ECO:0000269|PubMed:12554638, ECO:0000269|PubMed:12642614,
ECO:0000269|PubMed:12725728, ECO:0000269|PubMed:15201867,
ECO:0000269|PubMed:15964280, ECO:0000269|PubMed:21248204,
ECO:0000269|PubMed:8294515, ECO:0000269|PubMed:9700160}.
-!- INTERACTION:
Q03824:INP2; NbExp=3; IntAct=EBI-11659, EBI-27354;
P32526:KAR9; NbExp=2; IntAct=EBI-11659, EBI-9516;
P53141:MLC1; NbExp=3; IntAct=EBI-11659, EBI-10988;
P51534:SHE4; NbExp=2; IntAct=EBI-11659, EBI-17086;
P25591:VAC17; NbExp=7; IntAct=EBI-11659, EBI-21800;
-!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:8188749}. Bud
tip {ECO:0000269|PubMed:8188749}. Note=Concentrates to sites of
polarized growth, namely to the bud tip during S and G2 phases of
the cell cycle and to the bud neck during cytokinesis.
-!- DOMAIN: The myosin motor domain binds to actin.
-!- DOMAIN: The IQ domains provide the interaction surface for the
myosin light chain MLC1.
-!- DOMAIN: The coiled-coiled domain is necessary for dimerization.
-!- DOMAIN: The tail domain is a globular cargo-binding domain
involved in vectorial vesicle transport.
-!- MISCELLANEOUS: Present with 4339 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- MISCELLANEOUS: Moves with an average velocity of 3 um/s along
actin cables.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
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EMBL; M35532; AAA34810.1; -; Genomic_DNA.
EMBL; Z75234; CAA99646.1; -; Genomic_DNA.
EMBL; Z75235; CAA99648.1; -; Genomic_DNA.
EMBL; X90565; CAA62184.1; -; Genomic_DNA.
EMBL; Z49821; CAA89973.1; -; Genomic_DNA.
EMBL; BK006948; DAA11089.1; -; Genomic_DNA.
PIR; A38454; A38454.
RefSeq; NP_014971.1; NM_001183746.1.
PDB; 1M45; X-ray; 1.65 A; B=806-830.
PDB; 1M46; X-ray; 2.10 A; B=854-878.
PDB; 1N2D; X-ray; 2.00 A; C=806-853.
PDB; 2F6H; X-ray; 2.25 A; X=1152-1570.
PDBsum; 1M45; -.
PDBsum; 1M46; -.
PDBsum; 1N2D; -.
PDBsum; 2F6H; -.
ProteinModelPortal; P19524; -.
SMR; P19524; -.
BioGrid; 34711; 647.
DIP; DIP-2308N; -.
IntAct; P19524; 50.
MINT; P19524; -.
STRING; 4932.YOR326W; -.
CarbonylDB; P19524; -.
iPTMnet; P19524; -.
MaxQB; P19524; -.
PaxDb; P19524; -.
PRIDE; P19524; -.
EnsemblFungi; YOR326W; YOR326W; YOR326W.
GeneID; 854504; -.
KEGG; sce:YOR326W; -.
EuPathDB; FungiDB:YOR326W; -.
SGD; S000005853; MYO2.
GeneTree; ENSGT00910000144332; -.
HOGENOM; HOG000171839; -.
InParanoid; P19524; -.
KO; K10357; -.
OMA; MIPDFKQ; -.
OrthoDB; EOG092C04K7; -.
BioCyc; YEAST:G3O-33803-MONOMER; -.
EvolutionaryTrace; P19524; -.
PRO; PR:P19524; -.
Proteomes; UP000002311; Chromosome XV.
GO; GO:0032432; C:actin filament bundle; IMP:SGD.
GO; GO:0005935; C:cellular bud neck; IDA:SGD.
GO; GO:0005934; C:cellular bud tip; IDA:SGD.
GO; GO:0031941; C:filamentous actin; IDA:SGD.
GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
GO; GO:0043332; C:mating projection tip; IDA:SGD.
GO; GO:0071563; C:Myo2p-Vac17p-Vac8p transport complex; IPI:SGD.
GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
GO; GO:0030133; C:transport vesicle; IDA:SGD.
GO; GO:0031982; C:vesicle; IDA:SGD.
GO; GO:0051015; F:actin filament binding; IDA:SGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005516; F:calmodulin binding; IDA:SGD.
GO; GO:0000146; F:microfilament motor activity; IDA:SGD.
GO; GO:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
GO; GO:0007118; P:budding cell apical bud growth; IMP:SGD.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:SGD.
GO; GO:0048313; P:Golgi inheritance; IMP:SGD.
GO; GO:0007107; P:membrane addition at site of cytokinesis; IMP:SGD.
GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
GO; GO:0045033; P:peroxisome inheritance; IMP:SGD.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0009826; P:unidimensional cell growth; IMP:SGD.
GO; GO:0000011; P:vacuole inheritance; IMP:SGD.
GO; GO:0006904; P:vesicle docking involved in exocytosis; IGI:SGD.
GO; GO:0030050; P:vesicle transport along actin filament; IMP:SGD.
GO; GO:0016192; P:vesicle-mediated transport; IMP:SGD.
CDD; cd01380; MYSc_Myo5; 1.
Gene3D; 3.40.850.10; -; 3.
InterPro; IPR002710; Dilute_dom.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR004009; Myosin_N.
InterPro; IPR008989; Myosin_S1_N.
InterPro; IPR036103; MYSc_Myo5.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF01843; DIL; 1.
Pfam; PF00063; Myosin_head; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM01132; DIL; 1.
SMART; SM00015; IQ; 4.
SMART; SM00242; MYSc; 1.
SUPFAM; SSF50084; SSF50084; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51126; DILUTE; 1.
PROSITE; PS50096; IQ; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
PROSITE; PS51844; SH3_LIKE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Actin-binding; ATP-binding;
Calmodulin-binding; Cell cycle; Cell division; Coiled coil;
Complete proteome; Motor protein; Myosin; Nucleotide-binding;
Phosphoprotein; Protein transport; Reference proteome; Repeat;
Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 1574 Myosin-2.
/FTId=PRO_0000123489.
DOMAIN 4 57 Myosin N-terminal SH3-like.
{ECO:0000255|PROSITE-ProRule:PRU01190}.
DOMAIN 70 781 Myosin motor. {ECO:0000255|PROSITE-
ProRule:PRU00782}.
DOMAIN 784 806 IQ 1. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 807 831 IQ 2. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 832 855 IQ 3. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 856 879 IQ 4. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 880 902 IQ 5. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 903 932 IQ 6. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
DOMAIN 1226 1501 Dilute. {ECO:0000255|PROSITE-
ProRule:PRU00503}.
NP_BIND 164 171 ATP. {ECO:0000250}.
REGION 443 523 Actin-binding. {ECO:0000250}.
REGION 1087 1574 Non alpha-helical, tail domain.
COILED 933 1088
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 1097 1097 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 1121 1121 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MUTAGEN 511 511 E->K: In MYO2-66; disrupts actin binding.
{ECO:0000269|PubMed:8188749}.
MUTAGEN 1189 1189 V->A: In MYO2-573; causes a mitochondria
inheritance defect; when associated with
G-1288; M-1500; S-1529; G-1546 and R-
1559. {ECO:0000269|PubMed:12391144}.
MUTAGEN 1247 1247 S->G: Intragenic suppressor of MYO2-2.
{ECO:0000269|PubMed:12642614}.
MUTAGEN 1248 1248 G->D: In MYO2-2; causes a vacuole
inheritance defect.
{ECO:0000269|PubMed:9843969}.
MUTAGEN 1262 1262 V->A: Intragenic suppressor of MYO2-2.
{ECO:0000269|PubMed:12642614}.
MUTAGEN 1264 1264 F->S: Intragenic suppressor of MYO2-2.
{ECO:0000269|PubMed:12642614}.
MUTAGEN 1268 1268 S->P: Intragenic suppressor of MYO2-2.
{ECO:0000269|PubMed:12642614}.
MUTAGEN 1274 1274 T->M: Intragenic suppressor of MYO2-2.
{ECO:0000269|PubMed:12642614}.
MUTAGEN 1275 1275 F->S: Intragenic suppressor of MYO2-2.
{ECO:0000269|PubMed:12642614}.
MUTAGEN 1288 1288 V->A: Intragenic suppressor of MYO2-2.
{ECO:0000269|PubMed:12391144,
ECO:0000269|PubMed:12642614}.
MUTAGEN 1288 1288 V->G: In MYO2-573; causes a mitochondria
inheritance defect; when associated with
A-1189; M-1500; S-1529; G-1546 and R-
1559. {ECO:0000269|PubMed:12391144,
ECO:0000269|PubMed:12642614}.
MUTAGEN 1297 1297 D->G,N,V: Causes a vacuole inheritance
defect. {ECO:0000269|PubMed:10931864}.
MUTAGEN 1301 1301 L->P: Causes a vacuole inheritance
defect. {ECO:0000269|PubMed:10931864}.
MUTAGEN 1304 1304 N->D,S: Causes a vacuole inheritance
defect. {ECO:0000269|PubMed:10931864}.
MUTAGEN 1307 1307 N->D: Causes a vacuole inheritance
defect. {ECO:0000269|PubMed:10931864}.
MUTAGEN 1474 1474 L->S: In MYO2-338; abolishes interaction
with YPT11; when associated with G-1484
and G-1511.
{ECO:0000269|PubMed:12391144}.
MUTAGEN 1484 1484 E->G: In MYO2-338; abolishes interaction
with YPT11; when associated with S-1474
and G-1511.
{ECO:0000269|PubMed:12391144}.
MUTAGEN 1500 1500 K->M: In MYO2-573; causes a mitochondria
inheritance defect; when associated with
A-1189; G-1288; S-1529; G-1546 and R-
1559. {ECO:0000269|PubMed:12391144}.
MUTAGEN 1511 1511 D->G: In MYO2-338; abolishes interaction
with YPT11; when associated with S-1474
and G-1484.
{ECO:0000269|PubMed:12391144}.
MUTAGEN 1529 1529 P->S: In MYO2-573; causes a mitochondria
inheritance defect; when associated with
A-1189; G-1288; M-1500; G-1546 and R-
1559. {ECO:0000269|PubMed:12391144}.
MUTAGEN 1546 1546 E->G: In MYO2-573; causes a mitochondria
inheritance defect; when associated with
A-1189; G-1288; M-1500; S-1529 and R-
1559. {ECO:0000269|PubMed:12391144}.
MUTAGEN 1559 1559 K->R: In MYO2-573; causes a mitochondria
inheritance defect; when associated with
A-1189; G-1288; M-1500; S-1529 and G-
1546. {ECO:0000269|PubMed:12391144}.
HELIX 807 829 {ECO:0000244|PDB:1M45}.
HELIX 855 877 {ECO:0000244|PDB:1M46}.
HELIX 1153 1165 {ECO:0000244|PDB:2F6H}.
HELIX 1167 1176 {ECO:0000244|PDB:2F6H}.
TURN 1177 1181 {ECO:0000244|PDB:2F6H}.
HELIX 1195 1198 {ECO:0000244|PDB:2F6H}.
HELIX 1200 1214 {ECO:0000244|PDB:2F6H}.
HELIX 1218 1237 {ECO:0000244|PDB:2F6H}.
HELIX 1241 1243 {ECO:0000244|PDB:2F6H}.
HELIX 1244 1271 {ECO:0000244|PDB:2F6H}.
HELIX 1281 1325 {ECO:0000244|PDB:2F6H}.
TURN 1332 1335 {ECO:0000244|PDB:2F6H}.
HELIX 1355 1371 {ECO:0000244|PDB:2F6H}.
HELIX 1376 1399 {ECO:0000244|PDB:2F6H}.
HELIX 1407 1426 {ECO:0000244|PDB:2F6H}.
HELIX 1432 1435 {ECO:0000244|PDB:2F6H}.
HELIX 1437 1445 {ECO:0000244|PDB:2F6H}.
HELIX 1453 1462 {ECO:0000244|PDB:2F6H}.
TURN 1463 1465 {ECO:0000244|PDB:2F6H}.
HELIX 1468 1477 {ECO:0000244|PDB:2F6H}.
HELIX 1489 1504 {ECO:0000244|PDB:2F6H}.
HELIX 1505 1507 {ECO:0000244|PDB:2F6H}.
HELIX 1533 1536 {ECO:0000244|PDB:2F6H}.
HELIX 1556 1567 {ECO:0000244|PDB:2F6H}.
SEQUENCE 1574 AA; 180680 MW; 1F7E2887C1E59D54 CRC64;
MSFEVGTRCW YPHKELGWIG AEVIKNEFND GKYHLELQLE DDEIVSVDTK DLNNDKDQSL
PLLRNPPILE ATEDLTSLSY LNEPAVLHAI KQRYSQLNIY TYSGIVLIAT NPFDRVDQLY
TQDMIQAYAG KRRGELEPHL FAIAEEAYRL MKNDKQNQTI VVSGESGAGK TVSAKYIMRY
FASVEEENSA TVQHQVEMSE TEQKILATNP IMEAFGNAKT TRNDNSSRFG KYLEILFDKD
TSIIGARIRT YLLERSRLVY QPPIERNYHI FYQLMAGLPA QTKEELHLTD ASDYFYMNQG
GDTKINGIDD AKEYKITVDA LTLVGITKET QHQIFKILAA LLHIGNIEIK KTRNDASLSA
DEPNLKLACE LLGIDAYNFA KWVTKKQIIT RSEKIVSNLN YSQALVAKDS VAKFIYSALF
DWLVENINTV LCNPAVNDQI SSFIGVLDIY GFEHFEKNSF EQFCINYANE KLQQEFNQHV
FKLEQEEYVK EEIEWSFIEF NDNQPCIDLI ENKLGILSLL DEESRLPAGS DESWTQKLYQ
TLDKSPTNKV FSKPRFGQTK FIVSHYALDV AYDVEGFIEK NRDTVSDGHL EVLKASTNET
LINILEGLEK AAKKLEEAKK LELEQAGSKK PGPIRTVNRK PTLGSMFKQS LIELMNTINS
TNVHYIRCIK PNADKEAWQF DNLMVLSQLR ACGVLETIRI SCAGFPSRWT FEEFVLRYYI
LIPHEQWDLI FKKKETTEED IISVVKMILD ATVKDKSKYQ IGNTKIFFKA GMLAYLEKLR
SNKMHNSIVM IQKKIRAKYY RKQYLQISQA IKYLQNNIKG FIIRQRVNDE MKVNCATLLQ
AAYRGHSIRA NVFSVLRTIT NLQKKIRKEL KQRQLKQEHE YNAAVTIQSK VRTFEPRSRF
LRTKKDTVVV QSLIRRRAAQ RKLKQLKADA KSVNHLKEVS YKLENKVIEL TQNLASKVKE
NKEMTERIKE LQVQVEESAK LQETLENMKK EHLIDIDNQK SKDMELQKTI ENNLQSTEQT
LKDAQLELED MVKQHDELKE ESKKQLEELE QTKKTLVEYQ TLNGDLQNEV KSLKEEIARL
QTAMSLGTVT TSVLPQTPLK DVMGGGASNF NNMMLENSDL SPNDLNLKSR STPSSGNNHI
DSLSVDRENG VNATQINEEL YRLLEDTEIL NQEITEGLLK GFEVPDAGVA IQLSKRDVVY
PARILIIVLS EMWRFGLTKQ SESFLAQVLT TIQKVVTQLK GNDLIPSGVF WLANVRELYS
FVVFALNSIL TEETFKNGMT DEEYKEYVSL VTELKDDFEA LSYNIYNIWL KKLQKQLQKK
AINAVVISES LPGFSAGETS GFLNKIFANT EEYTMDDILT FFNSIYWCMK SFHIENEVFH
AVVTTLLNYV DAICFNELIM KRNFLSWKRG LQLNYNVTRL EEWCKTHGLT DGTECLQHLI
QTAKLLQVRK YTIEDIDILR GICYSLTPAQ LQKLISQYQV ADYESPIPQE ILRYVADIVK
KEAALSSSGN DSKGHEHSSS IFITPETGPF TDPFSLIKTR KFDQVEAYIP AWLSLPSTKR
IVDLVAQQVV QDGH


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